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Histone deacetylase 9 (HD9) (EC 3.5.1.98) (Histone deacetylase 7B) (HD7) (HD7b) (Histone deacetylase-related protein) (MEF2-interacting transcription repressor MITR)

 HDAC9_HUMAN             Reviewed;        1011 AA.
Q9UKV0; A7E2F3; B7Z4I4; B7Z917; B7Z928; B7Z940; C9JS87; E7EX34;
F8W9E0; O94845; O95028; Q2M2R6; Q86SL1; Q86US3;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
18-OCT-2001, sequence version 2.
27-SEP-2017, entry version 174.
RecName: Full=Histone deacetylase 9;
Short=HD9;
EC=3.5.1.98;
AltName: Full=Histone deacetylase 7B;
Short=HD7;
Short=HD7b;
AltName: Full=Histone deacetylase-related protein;
AltName: Full=MEF2-interacting transcription repressor MITR;
Name=HDAC9; Synonyms=HDAC7, HDAC7B, HDRP, KIAA0744, MITR;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 4), TISSUE SPECIFICITY,
INTERACTION WITH MEF2, FUNCTION, AND ENZYME REGULATION.
TISSUE=Brain;
PubMed=11535832; DOI=10.1073/pnas.191375098;
Zhou X., Marks P.A., Rifkind R.A., Richon V.M.;
"Cloning and characterization of a histone deacetylase, HDAC9.";
Proc. Natl. Acad. Sci. U.S.A. 98:10572-10577(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), TISSUE SPECIFICITY, AND
CHROMOSOMAL TRANSLOCATION WITH TGFB2.
TISSUE=Lens;
PubMed=12706107; DOI=10.1016/S0888-7543(03)00046-6;
David D., Cardoso J., Marques B., Marques R., Silva E.D., Santos H.,
Boavida M.G.;
"Molecular characterization of a familial translocation implicates
disruption of HDAC9 and possible position effect on TGFbeta2 in the
pathogenesis of Peters' anomaly.";
Genomics 81:489-503(2003).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 7), TISSUE SPECIFICITY,
ALTERNATIVE SPLICING (ISOFORMS 3; 6 AND 7), INTERACTION WITH ETV6;
NCOR1 AND BCL6, FUNCTION, SUBCELLULAR LOCATION, AND SUMOYLATION.
TISSUE=Brain;
PubMed=12590135; DOI=10.1074/jbc.M212935200;
Petrie K., Guidez F., Howell L., Healy L., Waxman S., Greaves M.,
Zelent A.;
"The histone deacetylase 9 gene encodes multiple protein isoforms.";
J. Biol. Chem. 278:16059-16072(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Brain;
PubMed=9872452; DOI=10.1093/dnares/5.5.277;
Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XI.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 5:277-286(1998).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 8; 9; 10 AND 11).
TISSUE=Brain, and Trachea;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 2-1011 (ISOFORM 6).
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 99-650 (ISOFORM 2).
TISSUE=Brain;
PubMed=10523670; DOI=10.1128/MCB.19.11.7816;
Wang A.H., Bertos N.R., Vezmar M., Pelletier N., Crosato M.,
Heng H.H., Th'ng J., Han J., Yang X.-J.;
"HDAC4, a human histone deacetylase related to yeast HDA1, is a
transcriptional corepressor.";
Mol. Cell. Biol. 19:7816-7827(1999).
[10]
IDENTIFICATION (ISOFORM 3), INTERACTION WITH HDAC1, AND FUNCTION.
PubMed=10487760; DOI=10.1093/emboj/18.18.5085;
Sparrow D.B., Miska E.A., Langley E., Reynaud-Deonauth S., Kotecha S.,
Towers N., Spohr G., Kouzarides T., Mohun T.J.;
"MEF-2 function is modified by a novel co-repressor, MITR.";
EMBO J. 18:5085-5098(1999).
[11]
IDENTIFICATION (ISOFORM 3), TISSUE SPECIFICITY, INTERACTION WITH HDAC1
AND HDAC3, AND FUNCTION.
PubMed=10655483; DOI=10.1073/pnas.97.3.1056;
Zhou X., Richon V.M., Rifkind R.A., Marks P.A.;
"Identification of a transcriptional repressor related to the
noncatalytic domain of histone deacetylases 4 and 5.";
Proc. Natl. Acad. Sci. U.S.A. 97:1056-1061(2000).
[12]
INTERACTION WITH MEF2.
PubMed=10487761; DOI=10.1093/emboj/18.18.5099;
Miska E.A., Karlsson C., Langley E., Nielsen S.J., Pines J.,
Kouzarides T.;
"HDAC4 deacetylase associates with and represses the MEF2
transcription factor.";
EMBO J. 18:5099-5107(1999).
[13]
SUMOYLATION.
PubMed=12032081; DOI=10.1093/emboj/21.11.2682;
Kirsh O., Seeler J.-S., Pichler A., Gast A., Mueller S., Miska E.,
Mathieu M., Harel-Bellan A., Kouzarides T., Melchior F., Dejean A.;
"The SUMO E3 ligase RanBP2 promotes modification of the HDAC4
deacetylase.";
EMBO J. 21:2682-2691(2002).
[14]
FUNCTION.
PubMed=16611996; DOI=10.1128/MCB.26.9.3550-3564.2006;
Morrison B.E., Majdzadeh N., Zhang X., Lyles A., Bassel-Duby R.,
Olson E.N., D'Mello S.R.;
"Neuroprotection by histone deacetylase-related protein.";
Mol. Cell. Biol. 26:3550-3564(2006).
[15]
INTERACTION WITH FOXP3.
PubMed=17360565; DOI=10.1073/pnas.0700298104;
Li B., Samanta A., Song X., Iacono K.T., Bembas K., Tao R., Basu S.,
Riley J.L., Hancock W.W., Shen Y., Saouaf S.J., Greene M.I.;
"FOXP3 interactions with histone acetyltransferase and class II
histone deacetylases are required for repression.";
Proc. Natl. Acad. Sci. U.S.A. 104:4571-4576(2007).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[17]
PHOSPHORYLATION.
PubMed=20188095; DOI=10.1016/j.febslet.2010.02.057;
Harrison B.C., Huynh K., Lundgaard G.L., Helmke S.M., Perryman M.B.,
McKinsey T.A.;
"Protein kinase C-related kinase targets nuclear localization signals
in a subset of class IIa histone deacetylases.";
FEBS Lett. 584:1103-1110(2010).
[18]
VARIANT THR-921.
PubMed=21248752; DOI=10.1038/nature09639;
Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P.,
Davies H., Jones D., Lin M.L., Teague J., Bignell G., Butler A.,
Cho J., Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C.,
Jia M., Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A.,
Mudie L., Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S.,
Kahnoski R.J., Anema J., Tuveson D.A., Perez-Mancera P.A.,
Mustonen V., Fischer A., Adams D.J., Rust A., Chan-On W., Subimerb C.,
Dykema K., Furge K., Campbell P.J., Teh B.T., Stratton M.R.,
Futreal P.A.;
"Exome sequencing identifies frequent mutation of the SWI/SNF complex
gene PBRM1 in renal carcinoma.";
Nature 469:539-542(2011).
-!- FUNCTION: Responsible for the deacetylation of lysine residues on
the N-terminal part of the core histones (H2A, H2B, H3 and H4).
Histone deacetylation gives a tag for epigenetic repression and
plays an important role in transcriptional regulation, cell cycle
progression and developmental events. Represses MEF2-dependent
transcription.
-!- FUNCTION: Isoform 3 lacks active site residues and therefore is
catalytically inactive. Represses MEF2-dependent transcription by
recruiting HDAC1 and/or HDAC3. Seems to inhibit skeletal
myogenesis and to be involved in heart development. Protects
neurons from apoptosis, both by inhibiting JUN phosphorylation by
MAPK10 and by repressing JUN transcription via HDAC1 recruitment
to JUN promoter.
-!- CATALYTIC ACTIVITY: Hydrolysis of an N(6)-acetyl-lysine residue of
a histone to yield a deacetylated histone.
-!- ENZYME REGULATION: Inhibited by Trichostatin A (TSA) and
suberoylanilide hydroxamic acid. {ECO:0000269|PubMed:11535832}.
-!- SUBUNIT: Homodimer. Interacts with CTBP1. The phosphorylated form
interacts with 14-3-3 (By similarity). Interacts with HDAC1 and
HDAC3, and probably with HDAC4 and HDAC5. Interacts with MEF2,
MAPK10, ETV6, NCOR1 and BCL6. Interacts with FOXP3 in the absence
of T-cell stimulation. {ECO:0000250|UniProtKB:Q99N13,
ECO:0000269|PubMed:10487760, ECO:0000269|PubMed:10487761,
ECO:0000269|PubMed:10655483, ECO:0000269|PubMed:11535832,
ECO:0000269|PubMed:12590135, ECO:0000269|PubMed:17360565}.
-!- INTERACTION:
P41182:BCL6; NbExp=2; IntAct=EBI-765444, EBI-765407;
P41212:ETV6; NbExp=3; IntAct=EBI-765476, EBI-1372759;
Q60974:Ncor1 (xeno); NbExp=3; IntAct=EBI-1372717, EBI-349004;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=11;
Comment=Additional isoforms seem to exist.;
Name=1;
IsoId=Q9UKV0-1; Sequence=Displayed;
Name=2;
IsoId=Q9UKV0-2; Sequence=VSP_002082;
Name=3; Synonyms=HDRP, MITR;
IsoId=Q9UKV0-3; Sequence=VSP_002083, VSP_002084;
Note=Major form in most tissues. Inactive due to lack of active
site residues.;
Name=4; Synonyms=HDAC9a;
IsoId=Q9UKV0-4; Sequence=VSP_002085, VSP_002086;
Name=5; Synonyms=HDAC9b, HDAC9fl;
IsoId=Q9UKV0-5; Sequence=VSP_023768;
Note=Contains a phosphotyrosine at position 1007. {ECO:0000305};
Name=6;
IsoId=Q9UKV0-6; Sequence=VSP_023766, VSP_023767, VSP_023768;
Note=Ref.8 (AAI11736) sequence differs from that shown due to a
frameshift in position 1021. Contains a phosphotyrosine at
position 966 (Probable). Excluded from the nucleus. Does not
interact with ETV6. {ECO:0000305};
Name=7;
IsoId=Q9UKV0-7; Sequence=VSP_023766, VSP_023768;
Name=8;
IsoId=Q9UKV0-8; Sequence=VSP_043428, VSP_023767, VSP_002083,
VSP_002084;
Note=No experimental confirmation available.;
Name=9;
IsoId=Q9UKV0-9; Sequence=VSP_023767, VSP_002083, VSP_002084;
Name=10;
IsoId=Q9UKV0-10; Sequence=VSP_046827, VSP_023766, VSP_002083,
VSP_002084;
Name=11;
IsoId=Q9UKV0-11; Sequence=VSP_046827, VSP_046828, VSP_023767,
VSP_002083, VSP_002084;
-!- TISSUE SPECIFICITY: Broadly expressed, with highest levels in
brain, heart, muscle and testis. Isoform 3 is present in human
bladder carcinoma cells (at protein level).
{ECO:0000269|PubMed:10655483, ECO:0000269|PubMed:11535832,
ECO:0000269|PubMed:12590135, ECO:0000269|PubMed:12706107}.
-!- PTM: Phosphorylated on Ser-220 and Ser-450; which promotes 14-3-3-
binding, impairs interaction with MEF2, and antagonizes
antimyogenic activity. Phosphorylated on Ser-240; which impairs
nuclear accumulation (By similarity). Isoform 7 is phosphorylated
on Tyr-1010. Phosphorylated by the PKC kinases PKN1 and PKN2,
impairing nuclear import. {ECO:0000250,
ECO:0000269|PubMed:20188095}.
-!- PTM: Sumoylated. {ECO:0000269|PubMed:12032081,
ECO:0000269|PubMed:12590135}.
-!- DISEASE: Note=A chromosomal aberration involving HDAC9 is found in
a family with Peters anomaly. Translocation t(1;7)(q41;p21) with
TGFB2 resulting in lack of HDAC9 protein.
{ECO:0000269|PubMed:12706107}.
-!- SIMILARITY: Belongs to the histone deacetylase family. HD type 2
subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA34464.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AY032737; AAK66821.1; -; mRNA.
EMBL; AY032738; AAK66822.1; -; mRNA.
EMBL; AJ459808; CAD30851.1; -; mRNA.
EMBL; AY197371; AAO27363.1; -; mRNA.
EMBL; AB018287; BAA34464.2; ALT_INIT; mRNA.
EMBL; AK297404; BAH12570.1; -; mRNA.
EMBL; AK304298; BAH14153.1; -; mRNA.
EMBL; AK304343; BAH14164.1; -; mRNA.
EMBL; AK304410; BAH14176.1; -; mRNA.
EMBL; AC002088; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC002124; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC002410; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC002433; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC004744; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC004994; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC005249; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC010082; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC074193; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC091697; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471073; EAW93702.1; -; Genomic_DNA.
EMBL; CH471073; EAW93703.1; -; Genomic_DNA.
EMBL; BC111735; AAI11736.1; ALT_FRAME; mRNA.
EMBL; BC150328; AAI50329.1; -; mRNA.
EMBL; BC152405; AAI52406.1; -; mRNA.
EMBL; AF124924; AAF04254.1; -; mRNA.
CCDS; CCDS47553.1; -. [Q9UKV0-7]
CCDS; CCDS47554.1; -. [Q9UKV0-5]
CCDS; CCDS47555.1; -. [Q9UKV0-1]
CCDS; CCDS47557.1; -. [Q9UKV0-3]
CCDS; CCDS56465.1; -. [Q9UKV0-8]
CCDS; CCDS56466.1; -. [Q9UKV0-9]
CCDS; CCDS56467.1; -. [Q9UKV0-10]
CCDS; CCDS56468.1; -. [Q9UKV0-11]
CCDS; CCDS83163.1; -. [Q9UKV0-6]
RefSeq; NP_001191073.1; NM_001204144.2. [Q9UKV0-8]
RefSeq; NP_001191074.1; NM_001204145.2. [Q9UKV0-9]
RefSeq; NP_001191075.1; NM_001204146.2.
RefSeq; NP_001191076.1; NM_001204147.2. [Q9UKV0-11]
RefSeq; NP_001191077.1; NM_001204148.2. [Q9UKV0-10]
RefSeq; NP_001308797.1; NM_001321868.1.
RefSeq; NP_001308798.1; NM_001321869.1.
RefSeq; NP_001308799.1; NM_001321870.1.
RefSeq; NP_001308800.1; NM_001321871.1.
RefSeq; NP_001308801.1; NM_001321872.1.
RefSeq; NP_001308802.1; NM_001321873.1.
RefSeq; NP_001308803.1; NM_001321874.1.
RefSeq; NP_001308804.1; NM_001321875.1.
RefSeq; NP_001308805.1; NM_001321876.1.
RefSeq; NP_001308806.1; NM_001321877.1. [Q9UKV0-6]
RefSeq; NP_001308807.1; NM_001321878.1.
RefSeq; NP_001308808.1; NM_001321879.1.
RefSeq; NP_001308813.1; NM_001321884.1.
RefSeq; NP_001308814.1; NM_001321885.1.
RefSeq; NP_001308815.1; NM_001321886.1.
RefSeq; NP_001308816.1; NM_001321887.1.
RefSeq; NP_001308817.1; NM_001321888.1.
RefSeq; NP_001308818.1; NM_001321889.1.
RefSeq; NP_001308819.1; NM_001321890.1.
RefSeq; NP_001308820.1; NM_001321891.1. [Q9UKV0-9]
RefSeq; NP_001308822.1; NM_001321893.1. [Q9UKV0-9]
RefSeq; NP_001308823.1; NM_001321894.1.
RefSeq; NP_001308824.1; NM_001321895.1.
RefSeq; NP_001308825.1; NM_001321896.1. [Q9UKV0-10]
RefSeq; NP_001308826.1; NM_001321897.1. [Q9UKV0-6]
RefSeq; NP_001308827.1; NM_001321898.1.
RefSeq; NP_001308828.1; NM_001321899.1.
RefSeq; NP_001308829.1; NM_001321900.1. [Q9UKV0-3]
RefSeq; NP_001308830.1; NM_001321901.1.
RefSeq; NP_001308831.1; NM_001321902.1.
RefSeq; NP_055522.1; NM_014707.3. [Q9UKV0-3]
RefSeq; NP_478056.1; NM_058176.2. [Q9UKV0-1]
RefSeq; NP_848510.1; NM_178423.2. [Q9UKV0-5]
RefSeq; NP_848512.1; NM_178425.3. [Q9UKV0-7]
RefSeq; XP_011513940.1; XM_011515638.2. [Q9UKV0-7]
RefSeq; XP_011513941.1; XM_011515639.2. [Q9UKV0-7]
RefSeq; XP_016868315.1; XM_017012826.1. [Q9UKV0-5]
RefSeq; XP_016868317.1; XM_017012828.1. [Q9UKV0-6]
UniGene; Hs.196054; -.
UniGene; Hs.444785; -.
ProteinModelPortal; Q9UKV0; -.
SMR; Q9UKV0; -.
BioGrid; 115083; 58.
DIP; DIP-39904N; -.
ELM; Q9UKV0; -.
IntAct; Q9UKV0; 29.
MINT; MINT-205121; -.
STRING; 9606.ENSP00000408617; -.
BindingDB; Q9UKV0; -.
ChEMBL; CHEMBL4145; -.
DrugBank; DB05015; Belinostat.
DrugBank; DB06603; Panobinostat.
DrugBank; DB00313; Valproic Acid.
GuidetoPHARMACOLOGY; 2620; -.
iPTMnet; Q9UKV0; -.
PhosphoSitePlus; Q9UKV0; -.
BioMuta; HDAC9; -.
DMDM; 19865267; -.
PaxDb; Q9UKV0; -.
PeptideAtlas; Q9UKV0; -.
PRIDE; Q9UKV0; -.
DNASU; 9734; -.
Ensembl; ENST00000401921; ENSP00000383912; ENSG00000048052. [Q9UKV0-6]
Ensembl; ENST00000405010; ENSP00000384382; ENSG00000048052. [Q9UKV0-3]
Ensembl; ENST00000406451; ENSP00000384657; ENSG00000048052. [Q9UKV0-5]
Ensembl; ENST00000417496; ENSP00000401669; ENSG00000048052. [Q9UKV0-8]
Ensembl; ENST00000428307; ENSP00000395655; ENSG00000048052. [Q9UKV0-9]
Ensembl; ENST00000432645; ENSP00000410337; ENSG00000048052. [Q9UKV0-1]
Ensembl; ENST00000441542; ENSP00000408617; ENSG00000048052. [Q9UKV0-7]
Ensembl; ENST00000456174; ENSP00000388568; ENSG00000048052. [Q9UKV0-10]
Ensembl; ENST00000524023; ENSP00000430036; ENSG00000048052. [Q9UKV0-11]
GeneID; 9734; -.
KEGG; hsa:9734; -.
UCSC; uc003sud.2; human. [Q9UKV0-1]
CTD; 9734; -.
DisGeNET; 9734; -.
EuPathDB; HostDB:ENSG00000048052.21; -.
GeneCards; HDAC9; -.
HGNC; HGNC:14065; HDAC9.
HPA; HPA028926; -.
MalaCards; HDAC9; -.
MIM; 606543; gene.
neXtProt; NX_Q9UKV0; -.
OpenTargets; ENSG00000048052; -.
Orphanet; 708; Peters anomaly.
PharmGKB; PA38377; -.
eggNOG; KOG1343; Eukaryota.
eggNOG; COG0123; LUCA.
GeneTree; ENSGT00530000062809; -.
HOGENOM; HOG000232065; -.
HOVERGEN; HBG057100; -.
InParanoid; Q9UKV0; -.
KO; K11409; -.
OMA; DSQKFFS; -.
OrthoDB; EOG091G0EQO; -.
PhylomeDB; Q9UKV0; -.
TreeFam; TF106174; -.
BRENDA; 3.5.1.98; 2681.
Reactome; R-HSA-2122947; NOTCH1 Intracellular Domain Regulates Transcription.
Reactome; R-HSA-2644606; Constitutive Signaling by NOTCH1 PEST Domain Mutants.
Reactome; R-HSA-2894862; Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
SIGNOR; Q9UKV0; -.
ChiTaRS; HDAC9; human.
GeneWiki; HDAC9; -.
GenomeRNAi; 9734; -.
PRO; PR:Q9UKV0; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000048052; -.
CleanEx; HS_HDAC7; -.
CleanEx; HS_HDAC9; -.
ExpressionAtlas; Q9UKV0; baseline and differential.
Genevisible; Q9UKV0; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0000118; C:histone deacetylase complex; TAS:UniProtKB.
GO; GO:0035097; C:histone methyltransferase complex; ISS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005667; C:transcription factor complex; IDA:BHF-UCL.
GO; GO:0004407; F:histone deacetylase activity; IDA:BHF-UCL.
GO; GO:0042826; F:histone deacetylase binding; IDA:BHF-UCL.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0032041; F:NAD-dependent histone deacetylase activity (H3-K14 specific); IEA:UniProtKB-EC.
GO; GO:0033558; F:protein deacetylase activity; IDA:BHF-UCL.
GO; GO:0005080; F:protein kinase C binding; IPI:UniProtKB.
GO; GO:0070491; F:repressing transcription factor binding; IDA:BHF-UCL.
GO; GO:0003714; F:transcription corepressor activity; ISS:BHF-UCL.
GO; GO:0008134; F:transcription factor binding; IDA:BHF-UCL.
GO; GO:0042113; P:B cell activation; TAS:UniProtKB.
GO; GO:0030183; P:B cell differentiation; TAS:UniProtKB.
GO; GO:0032869; P:cellular response to insulin stimulus; IDA:BHF-UCL.
GO; GO:0007507; P:heart development; ISS:BHF-UCL.
GO; GO:0016575; P:histone deacetylation; IDA:BHF-UCL.
GO; GO:0070932; P:histone H3 deacetylation; IDA:BHF-UCL.
GO; GO:0070933; P:histone H4 deacetylation; IDA:BHF-UCL.
GO; GO:0006954; P:inflammatory response; TAS:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:BHF-UCL.
GO; GO:0030182; P:neuron differentiation; IEA:Ensembl.
GO; GO:0034983; P:peptidyl-lysine deacetylation; IDA:BHF-UCL.
GO; GO:0090050; P:positive regulation of cell migration involved in sprouting angiogenesis; IMP:BHF-UCL.
GO; GO:0048742; P:regulation of skeletal muscle fiber development; ISS:UniProtKB.
GO; GO:0051153; P:regulation of striated muscle cell differentiation; ISS:UniProtKB.
GO; GO:0001975; P:response to amphetamine; IEA:Ensembl.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 3.40.800.20; -; 1.
InterPro; IPR000286; His_deacetylse.
InterPro; IPR023801; His_deacetylse_dom.
InterPro; IPR024643; Hist_deacetylase_Gln_rich_N.
InterPro; IPR017320; Histone_deAcase_II_euk.
PANTHER; PTHR10625; PTHR10625; 1.
Pfam; PF12203; HDAC4_Gln; 1.
Pfam; PF00850; Hist_deacetyl; 1.
PIRSF; PIRSF037911; HDAC_II_euk; 1.
PRINTS; PR01270; HDASUPER.
1: Evidence at protein level;
Alternative splicing; Chromatin regulator; Chromosomal rearrangement;
Complete proteome; Hydrolase; Metal-binding; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; Repressor; Transcription;
Transcription regulation; Ubl conjugation; Zinc.
CHAIN 1 1011 Histone deacetylase 9.
/FTId=PRO_0000114710.
REGION 23 27 Interaction with CTBP1. {ECO:0000250}.
REGION 136 154 Interaction with MEF2. {ECO:0000250}.
REGION 175 343 Interaction with MAPK10. {ECO:0000250}.
REGION 218 261 Interaction with ETV6.
{ECO:0000269|PubMed:12590135}.
REGION 631 978 Histone deacetylase.
ACT_SITE 783 783 {ECO:0000250}.
METAL 646 646 Zinc. {ECO:0000250}.
METAL 648 648 Zinc. {ECO:0000250}.
METAL 654 654 Zinc. {ECO:0000250}.
METAL 731 731 Zinc. {ECO:0000250}.
MOD_RES 22 22 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 220 220 Phosphoserine.
{ECO:0000250|UniProtKB:Q99N13}.
MOD_RES 240 240 Phosphoserine.
{ECO:0000250|UniProtKB:Q99N13}.
MOD_RES 451 451 Phosphoserine.
{ECO:0000250|UniProtKB:Q99N13}.
MOD_RES 554 554 Phosphoserine.
{ECO:0000250|UniProtKB:Q99N13}.
VAR_SEQ 1 31 Missing (in isoform 10 and isoform 11).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_046827.
VAR_SEQ 1 1 M -> MMSSPAQPDLMWNLVPWVLFCGCCRIFPDGVAGREQ
LLAQQRM (in isoform 8).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043428.
VAR_SEQ 88 88 K -> KLQQ (in isoform 6, isoform 7 and
isoform 10).
{ECO:0000303|PubMed:12590135,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_023766.
VAR_SEQ 177 178 Missing (in isoform 11).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_046828.
VAR_SEQ 218 261 Missing (in isoform 6, isoform 8, isoform
9 and isoform 11).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_023767.
VAR_SEQ 487 574 Missing (in isoform 2).
{ECO:0000303|PubMed:10523670}.
/FTId=VSP_002082.
VAR_SEQ 575 590 PFLEPTHTRALSVRQA -> VIGKDLAPGFVIKVII (in
isoform 3, isoform 8, isoform 9, isoform
10 and isoform 11).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9872452}.
/FTId=VSP_002083.
VAR_SEQ 591 1011 Missing (in isoform 3, isoform 8, isoform
9, isoform 10 and isoform 11).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9872452}.
/FTId=VSP_002084.
VAR_SEQ 861 879 GTGLGEGYNINIAWTGGLD -> RFISLEPHFYLYLSGNCI
A (in isoform 4).
{ECO:0000303|PubMed:11535832}.
/FTId=VSP_002085.
VAR_SEQ 880 1011 Missing (in isoform 4).
{ECO:0000303|PubMed:11535832}.
/FTId=VSP_002086.
VAR_SEQ 1006 1011 MSLKFS -> KYWKSVRMVAVPRGCALAGAQLQEETETVSA
LASLTVDVEQPFAQEDSRTAGEPMEEEPAL (in
isoform 5, isoform 6 and isoform 7).
{ECO:0000303|PubMed:12590135,
ECO:0000303|PubMed:12706107,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_023768.
VARIANT 921 921 P -> T (found in a renal cell carcinoma
sample; somatic mutation).
{ECO:0000269|PubMed:21248752}.
/FTId=VAR_064719.
CONFLICT 16 16 V -> A (in Ref. 5; BAH12570).
{ECO:0000305}.
CONFLICT 99 99 L -> I (in Ref. 9; AAF04254).
{ECO:0000305}.
CONFLICT 153 153 S -> I (in Ref. 5; BAH14164).
{ECO:0000305}.
CONFLICT 315 315 S -> F (in Ref. 5; BAH14176).
{ECO:0000305}.
CONFLICT 332 332 L -> M (in Ref. 5; BAH14164).
{ECO:0000305}.
CONFLICT 416 416 V -> F (in Ref. 5; BAH14164).
{ECO:0000305}.
CONFLICT 437 437 T -> P (in Ref. 9; AAF04254).
{ECO:0000305}.
CONFLICT 644 647 HQCV -> KPNS (in Ref. 9; AAF04254).
{ECO:0000305}.
CONFLICT 746 746 H -> R (in Ref. 3; AAO27363).
{ECO:0000305}.
SEQUENCE 1011 AA; 111297 MW; 43ED2785E73CD924 CRC64;
MHSMISSVDV KSEVPVGLEP ISPLDLRTDL RMMMPVVDPV VREKQLQQEL LLIQQQQQIQ
KQLLIAEFQK QHENLTRQHQ AQLQEHIKEL LAIKQQQELL EKEQKLEQQR QEQEVERHRR
EQQLPPLRGK DRGRERAVAS TEVKQKLQEF LLSKSATKDT PTNGKNHSVS RHPKLWYTAA
HHTSLDQSSP PLSGTSPSYK YTLPGAQDAK DDFPLRKTAS EPNLKVRSRL KQKVAERRSS
PLLRRKDGNV VTSFKKRMFE VTESSVSSSS PGSGPSSPNN GPTGSVTENE TSVLPPTPHA
EQMVSQQRIL IHEDSMNLLS LYTSPSLPNI TLGLPAVPSQ LNASNSLKEK QKCETQTLRQ
GVPLPGQYGG SIPASSSHPH VTLEGKPPNS SHQALLQHLL LKEQMRQQKL LVAGGVPLHP
QSPLATKERI SPGIRGTHKL PRHRPLNRTQ SAPLPQSTLA QLVIQQQHQQ FLEKQKQYQQ
QIHMNKLLSK SIEQLKQPGS HLEEAEEELQ GDQAMQEDRA PSSGNSTRSD SSACVDDTLG
QVGAVKVKEE PVDSDEDAQI QEMESGEQAA FMQQPFLEPT HTRALSVRQA PLAAVGMDGL
EKHRLVSRTH SSPAASVLPH PAMDRPLQPG SATGIAYDPL MLKHQCVCGN STTHPEHAGR
IQSIWSRLQE TGLLNKCERI QGRKASLEEI QLVHSEHHSL LYGTNPLDGQ KLDPRILLGD
DSQKFFSSLP CGGLGVDSDT IWNELHSSGA ARMAVGCVIE LASKVASGEL KNGFAVVRPP
GHHAEESTAM GFCFFNSVAI TAKYLRDQLN ISKILIVDLD VHHGNGTQQA FYADPSILYI
SLHRYDEGNF FPGSGAPNEV GTGLGEGYNI NIAWTGGLDP PMGDVEYLEA FRTIVKPVAK
EFDPDMVLVS AGFDALEGHT PPLGGYKVTA KCFGHLTKQL MTLADGRVVL ALEGGHDLTA
ICDASEACVN ALLGNELEPL AEDILHQSPN MNAVISLQKI IEIQSMSLKF S


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